data_4856 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural Insight into Human Zn(2+)-bound S100A2 from NMR and Homology Modeling ; _BMRB_accession_number 4856 _BMRB_flat_file_name bmr4856.str _Entry_type original _Submission_date 2000-10-13 _Accession_date 2000-10-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Two primary sets of signals in a ratio of ~4:1 are observed in the spectra of S100A2. These are attributed to cis-trans isomerism at Pro43. Separate chemical shift lists are provided for each isoform. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Randazzo Antonio . . 2 Chazin Walter J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 734 "13C chemical shifts" 402 "15N chemical shifts" 170 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-01-23 original author . stop_ _Original_release_date 2002-01-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural Insight into Human Zn(2+)-bound S100A2 from NMR and Homology Modeling' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21518228 _PubMed_ID 11606065 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Randazzo Antonio . . 2 Acklin Christian . . 3 Schafer Beat W. . 4 Heizmann Claus W. . 5 Chazin Walter J. . stop_ _Journal_abbreviation 'Biochem. Biophys. Res. Commun.' _Journal_volume 288 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 462 _Page_last 467 _Year 2001 _Details . loop_ _Keyword 'calcium-binding protein' 'proline isomerism' S100A2 'zinc-binding protein' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Proline isomerism leads to multiple folded conformations of calbindin D9k: direct evidence from two-dimensional 1H NMR specrtoscopy. Proc Natl Acad Sci USA. 1989 Apr;86(7):2195-8 ; _Citation_title 'Proline isomerism leads to multiple folded conformations of calbindin D9k: direct evidence from two-dimensional 1H NMR spectroscopy.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 2928325 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chazin 'W. J.' J. . 2 Kordel J. . . 3 Drakenberg T. . . 4 Thulin E. . . 5 Brodin P. . . 6 Grundstrom T. . . 7 Forsen S. . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 86 _Journal_issue 7 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 2195 _Page_last 2198 _Year 1989 _Details ; A complete analysis of calbindin D9k by two-dimensional 1H nuclear magnetic resonance spectroscopy has established the existence of two conformations for the folded protein in solution. Well-resolved major and minor resonances in a ratio of 3:1 are observed throughout the 1H NMR spectrum. Two-dimensional exchange experiments show that the major and minor species are related by an equilibrium process. Analysis of short proton-proton distances along the peptide backbone, identified by two-dimensional nuclear Overhauser effect spectroscopy, provides unambiguous evidence that the two forms of the folded protein differ only in the isomerization state of the peptide bond between Gly-42 and Pro-43. Cis-trans isomerism of Pro-43 is thereby directly identified as the cause of multiple conformations for the folded protein in solution. In addition, when Pro-43 is mutated to a glycine residue there is no indication of multiple conformations. These results provide evidence for the possibility of conformational heterogeneity in the native state of globular proteins. ; save_ ################################## # Molecular system description # ################################## save_S100A2 _Saveframe_category molecular_system _Mol_system_name 'S100A2 homodimer' _Abbreviation_common S100A2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'S100A2 subunit A' $CaBP 'S100A2 subunit B' $CaBP ZN-1 $ZN ZN-2 $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'S100A2 subunit A' 1 'S100A2 subunit B' stop_ loop_ _Biological_function calcium-binding zinc-binding stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CaBP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Calcium Binding Protein' _Abbreviation_common CaBP _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 97 _Mol_residue_sequence ; MCSSLEQALAVLVTTFHKYS CQEGDKFKLSKGEMKELLHK ELPSFVGEKVDEEGLKKLMG SLDENSDQQVDFQEYAVFLA LITVMCNDFFQGCPDRP ; loop_ _Residue_seq_code _Residue_label 1 MET 2 CYS 3 SER 4 SER 5 LEU 6 GLU 7 GLN 8 ALA 9 LEU 10 ALA 11 VAL 12 LEU 13 VAL 14 THR 15 THR 16 PHE 17 HIS 18 LYS 19 TYR 20 SER 21 CYS 22 GLN 23 GLU 24 GLY 25 ASP 26 LYS 27 PHE 28 LYS 29 LEU 30 SER 31 LYS 32 GLY 33 GLU 34 MET 35 LYS 36 GLU 37 LEU 38 LEU 39 HIS 40 LYS 41 GLU 42 LEU 43 PRO 44 SER 45 PHE 46 VAL 47 GLY 48 GLU 49 LYS 50 VAL 51 ASP 52 GLU 53 GLU 54 GLY 55 LEU 56 LYS 57 LYS 58 LEU 59 MET 60 GLY 61 SER 62 LEU 63 ASP 64 GLU 65 ASN 66 SER 67 ASP 68 GLN 69 GLN 70 VAL 71 ASP 72 PHE 73 GLN 74 GLU 75 TYR 76 ALA 77 VAL 78 PHE 79 LEU 80 ALA 81 LEU 82 ILE 83 THR 84 VAL 85 MET 86 CYS 87 ASN 88 ASP 89 PHE 90 PHE 91 GLN 92 GLY 93 CYS 94 PRO 95 ASP 96 ARG 97 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 4DUQ "The Structure Of Ca2+-loaded S100a2 At 1.3a Resolution" 100.00 98 96.91 96.91 1.11e-60 EMBL CAA69033 "S100A2 [Homo sapiens]" 100.00 97 100.00 100.00 3.02e-63 GB AAH02829 "S100 calcium binding protein A2 [Homo sapiens]" 100.00 98 100.00 100.00 2.79e-63 GB AAI05788 "S100 calcium binding protein A2 [Homo sapiens]" 100.00 98 100.00 100.00 2.79e-63 GB AIC49664 "S100A2, partial [synthetic construct]" 100.00 97 100.00 100.00 3.02e-63 GB EAW53305 "S100 calcium binding protein A2 [Homo sapiens]" 100.00 98 100.00 100.00 2.79e-63 REF NP_005969 "protein S100-A2 [Homo sapiens]" 100.00 97 100.00 100.00 3.02e-63 REF XP_001110911 "PREDICTED: protein S100-A2-like isoform 1 [Macaca mulatta]" 100.00 98 97.94 98.97 9.05e-62 REF XP_001110950 "PREDICTED: protein S100-A2-like isoform 2 [Macaca mulatta]" 100.00 98 97.94 98.97 9.05e-62 REF XP_001139314 "PREDICTED: protein S100-A2 [Pan troglodytes]" 100.00 98 98.97 100.00 8.22e-63 REF XP_001139552 "PREDICTED: protein S100-A2 [Pan troglodytes]" 100.00 98 98.97 100.00 8.22e-63 SP P29034 "RecName: Full=Protein S100-A2; AltName: Full=CAN19; AltName: Full=Protein S-100L; AltName: Full=S100 calcium-binding protein A2" 100.00 98 100.00 100.00 2.79e-63 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 21 14:17:05 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CaBP human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $CaBP 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CaBP . mM 0.5 1.5 '[U-95% 13C; U-90% 15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CaBP . mM 0.5 1.5 '[U-90% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name FELIX _Version 98 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_15N-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _Sample_label . save_ save_13C-HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-HSQC _Sample_label . save_ save_C(CC-CO)NH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name C(CC-CO)NH-TOCSY _Sample_label . save_ save_H(CC-CO)NH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name H(CC-CO)NH-TOCSY _Sample_label . save_ save_HBHA(CBCACO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CBCACO)NH _Sample_label . save_ save_{1H}-15N_NOE_9 _Saveframe_category NMR_applied_experiment _Experiment_name '{1H}-15N NOE' _Sample_label . save_ save_NOESY-15N_HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name 'NOESY-15N HSQC' _Sample_label . save_ save_TOCSY-15N_HSQC_11 _Saveframe_category NMR_applied_experiment _Experiment_name 'TOCSY-15N HSQC' _Sample_label . save_ ####################### # Sample conditions # ####################### save_cond1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.2 n/a temperature 300 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . direct . . . 0.251449530 H2O H 1 proton ppm 4.73 internal direct cylindrical internal parallel_to_Bo . DSS N 15 'methyl protons' ppm 0.0 . direct . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_major _Saveframe_category assigned_chemical_shifts _Details 'S100A2 major isoform' loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'S100A2 subunit A' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 CYS H H 8.52 . 1 2 . 2 CYS HA H 4.55 . 1 3 . 2 CYS HB2 H 2.86 . 2 4 . 2 CYS HB3 H 2.94 . 2 5 . 2 CYS CA C 58.5 . 1 6 . 2 CYS CB C 28.5 . 1 7 . 2 CYS N N 121.3 . 1 8 . 3 SER H H 8.94 . 1 9 . 3 SER HA H 4.65 . 1 10 . 3 SER HB2 H 3.82 . 2 11 . 3 SER HB3 H 4.35 . 2 12 . 3 SER CA C 57.4 . 2 13 . 3 SER CB C 65.1 . 1 14 . 3 SER N N 119.3 . 1 15 . 4 SER H H 8.75 . 1 16 . 4 SER CA C 60.2 . 1 17 . 4 SER N N 117.3 . 1 18 . 7 GLN H H 8.06 . 1 19 . 7 GLN HA H 4.07 . 1 20 . 7 GLN HB2 H 2.15 . 1 21 . 7 GLN HB3 H 2.15 . 1 22 . 7 GLN HG2 H 2.48 . 2 23 . 7 GLN HG3 H 2.38 . 2 24 . 7 GLN CA C 58.7 . 1 25 . 7 GLN CB C 28.2 . 1 26 . 7 GLN CG C 33.9 . 1 27 . 7 GLN N N 118.0 . 1 28 . 8 ALA H H 8.21 . 1 29 . 8 ALA HA H 4.10 . 1 30 . 8 ALA HB H 1.55 . 1 31 . 8 ALA CA C 54.9 . 1 32 . 8 ALA CB C 17.1 . 1 33 . 8 ALA N N 123.0 . 1 34 . 9 LEU H H 8.38 . 1 35 . 9 LEU CA C 57.7 . 1 36 . 9 LEU N N 117.8 . 1 37 . 10 ALA H H 8.02 . 1 38 . 10 ALA HA H 4.04 . 1 39 . 10 ALA HB H 1.60 . 1 40 . 10 ALA CA C 55.5 . 1 41 . 10 ALA CB C 17.3 . 1 42 . 10 ALA N N 121.0 . 1 43 . 11 VAL H H 7.98 . 1 44 . 11 VAL HA H 3.81 . 1 45 . 11 VAL HB H 2.37 . 1 46 . 11 VAL HG1 H 0.78 . 2 47 . 11 VAL HG2 H 1.16 . 2 48 . 11 VAL CA C 66.5 . 1 49 . 11 VAL CB C 30.9 . 1 50 . 11 VAL CG1 C 20.4 . 2 51 . 11 VAL CG2 C 22.5 . 2 52 . 11 VAL N N 120.4 . 1 53 . 12 LEU H H 8.30 . 1 54 . 12 LEU HA H 3.95 . 1 55 . 12 LEU CA C 60.5 . 1 56 . 12 LEU CB C 44.9 . 1 57 . 12 LEU N N 124.26 . 1 58 . 13 VAL H H 8.15 . 1 59 . 13 VAL HA H 3.63 . 1 60 . 13 VAL HB H 1.98 . 1 61 . 13 VAL HG1 H 0.44 . 2 62 . 13 VAL HG2 H 0.60 . 2 63 . 13 VAL CA C 66.9 . 1 64 . 13 VAL CB C 31.8 . 1 65 . 13 VAL CG1 C 20.6 . 2 66 . 13 VAL CG2 C 22.6 . 2 67 . 13 VAL N N 120.2 . 1 68 . 14 THR H H 8.92 . 1 69 . 14 THR HA H 4.20 . 1 70 . 14 THR HB H 3.90 . 1 71 . 14 THR HG2 H 1.27 . 1 72 . 14 THR CA C 66.5 . 1 73 . 14 THR CB C 68.7 . 1 74 . 14 THR CG2 C 21.4 . 1 75 . 14 THR N N 116.2 . 1 76 . 15 THR H H 8.47 . 1 77 . 15 THR HA H 4.28 . 1 78 . 15 THR HB H 3.90 . 1 79 . 15 THR HG2 H 1.39 . 1 80 . 15 THR CA C 67.9 . 1 81 . 15 THR CG2 C 21.3 . 1 82 . 15 THR N N 112.2 . 1 83 . 16 PHE H H 7.28 . 1 84 . 16 PHE HA H 3.63 . 1 85 . 16 PHE HB2 H 3.28 . 1 86 . 16 PHE HB3 H 3.28 . 1 87 . 16 PHE CA C 62.0 . 1 88 . 16 PHE CB C 39.1 . 1 89 . 16 PHE N N 122.1 . 1 90 . 17 HIS H H 8.24 . 1 91 . 17 HIS CA C 57.7 . 1 92 . 17 HIS CB C 29.4 . 1 93 . 17 HIS N N 115.8 . 1 94 . 18 LYS H H 7.96 . 1 95 . 18 LYS HA H 3.80 . 1 96 . 18 LYS HB2 H 1.91 . 1 97 . 18 LYS HB3 H 1.91 . 1 98 . 18 LYS HG2 H 1.50 . 4 99 . 18 LYS HG3 H 1.50 . 4 100 . 18 LYS HD2 H 1.50 . 4 101 . 18 LYS HD3 H 1.50 . 4 102 . 18 LYS HE2 H 2.76 . 1 103 . 18 LYS HE3 H 2.76 . 1 104 . 18 LYS CA C 59.1 . 1 105 . 18 LYS CB C 32.1 . 1 106 . 18 LYS CG C 24.2 . 1 107 . 18 LYS CD C 29.2 . 1 108 . 18 LYS CE C 41.7 . 1 109 . 18 LYS N N 119.7 . 1 110 . 19 TYR H H 7.05 . 1 111 . 19 TYR HA H 4.17 . 1 112 . 19 TYR HB2 H 2.42 . 1 113 . 19 TYR HB3 H 2.91 . 1 114 . 19 TYR CA C 59.4 . 1 115 . 19 TYR CB C 40.1 . 1 116 . 19 TYR N N 114.1 . 1 117 . 21 CYS H H 9.15 . 1 118 . 21 CYS HA H 4.11 . 1 119 . 21 CYS CA C 57.8 . 1 120 . 21 CYS N N 123.7 . 1 121 . 22 GLN H H 7.59 . 1 122 . 22 GLN CA C 59.3 . 1 123 . 22 GLN CB C 28.2 . 1 124 . 22 GLN N N 115.6 . 1 125 . 24 GLY H H 8.38 . 1 126 . 24 GLY HA2 H 3.87 . 2 127 . 24 GLY HA3 H 3.68 . 2 128 . 24 GLY CA C 46.3 . 1 129 . 24 GLY N N 112.0 . 1 130 . 25 ASP H H 8.29 . 1 131 . 25 ASP CA C 53.7 . 1 132 . 25 ASP CB C 41.0 . 1 133 . 25 ASP N N 123.1 . 1 134 . 28 LYS H H 7.75 . 1 135 . 28 LYS CA C 55.5 . 1 136 . 28 LYS CB C 29.2 . 1 137 . 28 LYS N N 119.3 . 1 138 . 29 LEU H H 7.67 . 1 139 . 29 LEU N N 115.3 . 1 140 . 30 SER H H 9.13 . 1 141 . 30 SER HA H 4.90 . 1 142 . 30 SER HB2 H 4.41 . 2 143 . 30 SER HB3 H 3.95 . 2 144 . 30 SER CA C 57.2 . 1 145 . 30 SER CB C 64.7 . 1 146 . 30 SER N N 119.8 . 1 147 . 31 LYS H H 8.94 . 1 148 . 31 LYS HA H 3.79 . 1 149 . 31 LYS CA C 61.3 . 1 150 . 31 LYS N N 122.3 . 1 151 . 32 GLY H H 8.90 . 1 152 . 32 GLY HA2 H 3.80 . 2 153 . 32 GLY HA3 H 3.98 . 2 154 . 32 GLY CA C 46.8 . 1 155 . 32 GLY N N 105.9 . 1 156 . 33 GLU H H 7.87 . 1 157 . 33 GLU HA H 4.18 . 1 158 . 33 GLU HB2 H 2.32 . 1 159 . 33 GLU HB3 H 2.32 . 1 160 . 33 GLU HG2 H 2.38 . 1 161 . 33 GLU HG3 H 2.38 . 1 162 . 33 GLU CA C 58.4 . 1 163 . 33 GLU CB C 29.3 . 1 164 . 33 GLU CG C 36.6 . 1 165 . 33 GLU N N 123.8 . 1 166 . 34 MET H H 8.51 . 1 167 . 34 MET HA H 4.00 . 1 168 . 34 MET HG2 H 2.27 . 1 169 . 34 MET HG3 H 2.13 . 1 170 . 34 MET CA C 57.7 . 1 171 . 34 MET CB C 31.5 . 1 172 . 34 MET CG C 32.4 . 1 173 . 34 MET N N 120.2 . 1 174 . 35 LYS H H 8.06 . 1 175 . 35 LYS HA H 3.55 . 1 176 . 35 LYS HB2 H 1.93 . 1 177 . 35 LYS HB3 H 1.93 . 1 178 . 35 LYS HG2 H 1.58 . 4 179 . 35 LYS HG3 H 1.58 . 4 180 . 35 LYS HD2 H 1.58 . 4 181 . 35 LYS HD3 H 1.58 . 4 182 . 35 LYS CA C 60.7 . 1 183 . 35 LYS N N 118.8 . 1 184 . 36 GLU H H 7.26 . 1 185 . 36 GLU HA H 4.03 . 1 186 . 36 GLU HB2 H 1.95 . 2 187 . 36 GLU HB3 H 2.12 . 2 188 . 36 GLU HG2 H 2.37 . 1 189 . 36 GLU HG3 H 2.37 . 1 190 . 36 GLU CA C 59.2 . 1 191 . 36 GLU CB C 28.9 . 1 192 . 36 GLU CG C 35.2 . 1 193 . 36 GLU N N 119.0 . 1 194 . 37 LEU H H 8.00 . 1 195 . 37 LEU HA H 4.61 . 1 196 . 37 LEU HB2 H 1.69 . 4 197 . 37 LEU HB3 H 1.69 . 4 198 . 37 LEU HG H 1.69 . 4 199 . 37 LEU HD1 H 1.69 . 4 200 . 37 LEU HD2 H 1.69 . 4 201 . 37 LEU CA C 59.1 . 1 202 . 37 LEU CB C 41.7 . 1 203 . 37 LEU N N 122.0 . 1 204 . 38 LEU H H 8.16 . 1 205 . 38 LEU HA H 3.55 . 1 206 . 38 LEU HB2 H 1.88 . 1 207 . 38 LEU HB3 H 1.88 . 1 208 . 38 LEU CA C 58.17 . 1 209 . 38 LEU CB C 41.55 . 1 210 . 38 LEU N N 118.7 . 1 211 . 39 HIS H H 7.66 . 1 212 . 39 HIS HA H 4.07 . 1 213 . 39 HIS HB2 H 3.09 . 1 214 . 39 HIS HB3 H 3.09 . 1 215 . 39 HIS CA C 59.3 . 1 216 . 39 HIS CB C 29.3 . 1 217 . 39 HIS N N 113.9 . 1 218 . 40 LYS H H 8.34 . 1 219 . 40 LYS HA H 4.10 . 1 220 . 40 LYS HB2 H 2.04 . 1 221 . 40 LYS HB3 H 2.04 . 1 222 . 40 LYS HG2 H 1.74 . 4 223 . 40 LYS HG3 H 1.74 . 4 224 . 40 LYS HD2 H 1.47 . 4 225 . 40 LYS HD3 H 1.47 . 4 226 . 40 LYS HE2 H 3.00 . 1 227 . 40 LYS HE3 H 3.00 . 1 228 . 40 LYS CA C 58.1 . 1 229 . 40 LYS CB C 33.4 . 1 230 . 40 LYS CG C 25.4 . 1 231 . 40 LYS CD C 28.4 . 1 232 . 40 LYS CE C 41.9 . 1 233 . 40 LYS N N 116.0 . 1 234 . 41 GLU H H 8.77 . 1 235 . 41 GLU HA H 4.66 . 1 236 . 41 GLU HB2 H 1.94 . 1 237 . 41 GLU HB3 H 1.94 . 1 238 . 41 GLU CA C 55.4 . 1 239 . 41 GLU CB C 30.3 . 1 240 . 41 GLU CG C 34.9 . 1 241 . 42 LEU H H 7.29 . 1 242 . 42 LEU HA H 5.08 . 1 243 . 42 LEU HB2 H 2.12 . 1 244 . 42 LEU CA C 52.3 . 1 245 . 42 LEU CB C 41.5 . 1 246 . 42 LEU N N 118.2 . 1 247 . 45 PHE H H 8.08 . 1 248 . 45 PHE HA H 4.44 . 1 249 . 45 PHE HB2 H 2.97 . 2 250 . 45 PHE HB3 H 3.07 . 2 251 . 45 PHE CA C 57.6 . 1 252 . 45 PHE CB C 38.3 . 1 253 . 45 PHE N N 122.2 . 1 254 . 46 VAL H H 7.78 . 1 255 . 46 VAL HA H 3.99 . 1 256 . 46 VAL HB H 2.07 . 1 257 . 46 VAL HG1 H 0.76 . 2 258 . 46 VAL HG2 H 0.64 . 2 259 . 46 VAL CA C 62.5 . 1 260 . 46 VAL CB C 32.1 . 1 261 . 46 VAL CG1 C 20.7 . 1 262 . 46 VAL CG2 C 20.7 . 1 263 . 46 VAL N N 114.2 . 1 264 . 47 GLY H H 7.85 . 1 265 . 47 GLY HA2 H 3.93 . 2 266 . 47 GLY HA3 H 4.07 . 2 267 . 47 GLY CA C 46.2 . 1 268 . 47 GLY N N 108.4 . 1 269 . 48 GLU H H 8.02 . 1 270 . 48 GLU HA H 4.31 . 1 271 . 48 GLU HB2 H 2.05 . 1 272 . 48 GLU HB3 H 2.05 . 1 273 . 48 GLU HG2 H 2.25 . 1 274 . 48 GLU HG3 H 2.25 . 1 275 . 48 GLU CA C 57.5 . 1 276 . 48 GLU CB C 29.9 . 1 277 . 48 GLU CG C 36.0 . 1 278 . 48 GLU N N 118.0 . 1 279 . 49 LYS H H 7.92 . 1 280 . 49 LYS HA H 4.44 . 1 281 . 49 LYS HB2 H 1.67 . 2 282 . 49 LYS HB3 H 1.83 . 2 283 . 49 LYS HG2 H 1.56 . 4 284 . 49 LYS HG3 H 1.56 . 4 285 . 49 LYS HD2 H 1.28 . 4 286 . 49 LYS HD3 H 1.28 . 4 287 . 49 LYS HE2 H 2.86 . 1 288 . 49 LYS HE3 H 2.86 . 1 289 . 49 LYS CA C 55.9 . 1 290 . 49 LYS CB C 32.7 . 1 291 . 49 LYS CG C 24.1 . 4 292 . 49 LYS CD C 28.3 . 4 293 . 49 LYS CE C 42.2 . 1 294 . 49 LYS N N 118.3 . 1 295 . 50 VAL H H 7.47 . 1 296 . 50 VAL HA H 4.08 . 1 297 . 50 VAL HB H 2.09 . 1 298 . 50 VAL HG1 H 0.90 . 1 299 . 50 VAL HG2 H 0.90 . 1 300 . 50 VAL CA C 62.2 . 1 301 . 50 VAL CB C 32.6 . 1 302 . 50 VAL CG1 C 20.5 . 1 303 . 50 VAL CG2 C 20.5 . 1 304 . 50 VAL N N 117.4 . 1 305 . 51 ASP H H 8.16 . 1 306 . 51 ASP HA H 4.69 . 1 307 . 51 ASP HB2 H 2.60 . 2 308 . 51 ASP HB3 H 2.81 . 2 309 . 51 ASP CA C 53.5 . 1 310 . 51 ASP CB C 40.9 . 1 311 . 51 ASP N N 121.2 . 1 312 . 52 GLU H H 8.05 . 1 313 . 52 GLU HA H 4.07 . 1 314 . 52 GLU HB2 H 2.15 . 1 315 . 52 GLU HB3 H 2.15 . 1 316 . 52 GLU HG2 H 2.26 . 2 317 . 52 GLU HG3 H 2.37 . 2 318 . 52 GLU CA C 58.1 . 1 319 . 52 GLU CB C 29.5 . 1 320 . 52 GLU CG C 36.4 . 1 321 . 52 GLU N N 123.4 . 1 322 . 53 GLU H H 8.69 . 1 323 . 53 GLU HA H 3.90 . 1 324 . 53 GLU HB2 H 2.00 . 1 325 . 53 GLU HB3 H 2.00 . 1 326 . 53 GLU HG2 H 2.25 . 1 327 . 53 GLU HG3 H 2.25 . 1 328 . 53 GLU CA C 59.4 . 1 329 . 53 GLU CB C 29.3 . 1 330 . 53 GLU CG C 35.6 . 1 331 . 53 GLU N N 123.0 . 1 332 . 54 GLY H H 8.83 . 1 333 . 54 GLY HA2 H 3.78 . 2 334 . 54 GLY HA3 H 3.93 . 2 335 . 54 GLY CA C 47.2 . 1 336 . 54 GLY N N 108.4 . 1 337 . 55 LEU H H 7.90 . 1 338 . 55 LEU CA C 57.3 . 1 339 . 55 LEU CB C 41.5 . 1 340 . 55 LEU N N 124.0 . 1 341 . 56 LYS H H 8.22 . 1 342 . 56 LYS HA H 3.85 . 1 343 . 56 LYS HB2 H 1.80 . 4 344 . 56 LYS HB3 H 1.80 . 4 345 . 56 LYS HG2 H 1.80 . 4 346 . 56 LYS HG3 H 1.80 . 4 347 . 56 LYS HD2 H 1.80 . 4 348 . 56 LYS HD3 H 1.80 . 4 349 . 56 LYS CA C 59.7 . 1 350 . 56 LYS CB C 31.8 . 1 351 . 56 LYS CG C 24.5 . 4 352 . 56 LYS CD C 24.5 . 4 353 . 56 LYS N N 120.0 . 1 354 . 57 LYS H H 7.96 . 1 355 . 57 LYS HA H 4.01 . 1 356 . 57 LYS HB2 H 1.84 . 1 357 . 57 LYS HB3 H 1.84 . 1 358 . 57 LYS HG2 H 1.59 . 4 359 . 57 LYS HG3 H 1.59 . 4 360 . 57 LYS HD2 H 1.33 . 4 361 . 57 LYS HD3 H 1.48 . 4 362 . 57 LYS HE2 H 2.88 . 1 363 . 57 LYS HE3 H 2.88 . 1 364 . 57 LYS CA C 59.2 . 1 365 . 57 LYS CB C 31.9 . 1 366 . 57 LYS CG C 24.3 . 1 367 . 57 LYS CD C 28.7 . 1 368 . 57 LYS CE C 41.6 . 1 369 . 57 LYS N N 119.8 . 1 370 . 58 LEU H H 7.64 . 1 371 . 58 LEU HA H 4.13 . 1 372 . 58 LEU HB2 H 1.70 . 4 373 . 58 LEU HB3 H 1.70 . 4 374 . 58 LEU HG H 1.70 . 4 375 . 58 LEU CA C 58.1 . 1 376 . 58 LEU CG C 24.3 . 1 377 . 58 LEU N N 121.5 . 1 378 . 59 MET H H 8.85 . 1 379 . 59 MET HA H 4.28 . 1 380 . 59 MET HB2 H 2.14 . 1 381 . 59 MET HB3 H 2.14 . 1 382 . 59 MET HG2 H 2.50 . 2 383 . 59 MET HG3 H 2.70 . 2 384 . 59 MET CA C 57.3 . 1 385 . 59 MET CB C 30.8 . 1 386 . 59 MET CG C 32.5 . 1 387 . 59 MET N N 117.7 . 1 388 . 60 GLY H H 8.28 . 1 389 . 60 GLY HA2 H 3.96 . 1 390 . 60 GLY HA3 H 3.96 . 1 391 . 60 GLY CA C 46.5 . 1 392 . 60 GLY N N 107.8 . 1 393 . 61 SER H H 7.78 . 1 394 . 61 SER HA H 4.73 . 1 395 . 61 SER HB2 H 4.12 . 1 396 . 61 SER HB3 H 4.12 . 1 397 . 61 SER CA C 61.1 . 1 398 . 61 SER CB C 62.7 . 1 399 . 61 SER N N 117.3 . 1 400 . 62 LEU H H 7.53 . 1 401 . 62 LEU HA H 4.14 . 1 402 . 62 LEU HB2 H 1.90 . 4 403 . 62 LEU HB3 H 1.77 . 4 404 . 62 LEU HG H 1.77 . 4 405 . 62 LEU HD1 H 1.77 . 4 406 . 62 LEU HD2 H 1.77 . 4 407 . 62 LEU CA C 56.3 . 1 408 . 62 LEU CB C 40.4 . 1 409 . 62 LEU N N 121.5 . 1 410 . 63 ASP H H 7.39 . 1 411 . 63 ASP HA H 4.47 . 1 412 . 63 ASP HB2 H 2.60 . 2 413 . 63 ASP HB3 H 2.76 . 2 414 . 63 ASP CA C 55.1 . 1 415 . 63 ASP CB C 41.1 . 1 416 . 63 ASP N N 116.2 . 1 417 . 64 GLU H H 7.47 . 1 418 . 64 GLU HA H 4.18 . 1 419 . 64 GLU HB2 H 1.98 . 1 420 . 64 GLU HB3 H 1.98 . 1 421 . 64 GLU HG2 H 2.18 . 1 422 . 64 GLU HG3 H 2.18 . 1 423 . 64 GLU CA C 56.2 . 1 424 . 64 GLU CB C 30.2 . 1 425 . 64 GLU CG C 35.7 . 1 426 . 64 GLU N N 119.5 . 1 427 . 65 ASN H H 8.35 . 1 428 . 65 ASN HA H 4.70 . 1 429 . 65 ASN HB2 H 2.89 . 2 430 . 65 ASN HB3 H 2.73 . 2 431 . 65 ASN CA C 53.3 . 1 432 . 65 ASN CB C 37.8 . 1 433 . 65 ASN N N 118.7 . 1 434 . 66 SER H H 8.02 . 1 435 . 66 SER HA H 4.73 . 1 436 . 66 SER HB2 H 4.12 . 1 437 . 66 SER HB3 H 4.12 . 1 438 . 66 SER CA C 61.1 . 1 439 . 66 SER CB C 63.3 . 1 440 . 66 SER N N 115.2 . 1 441 . 67 ASP H H 8.57 . 1 442 . 67 ASP HA H 4.65 . 1 443 . 67 ASP HB2 H 2.70 . 1 444 . 67 ASP HB3 H 2.70 . 1 445 . 67 ASP CA C 54.1 . 1 446 . 67 ASP CB C 40.2 . 1 447 . 67 ASP N N 118.3 . 1 448 . 68 GLN H H 7.90 . 1 449 . 68 GLN HA H 4.23 . 1 450 . 68 GLN HB2 H 2.11 . 1 451 . 68 GLN HB3 H 2.11 . 1 452 . 68 GLN HG2 H 2.49 . 1 453 . 68 GLN HG3 H 2.49 . 1 454 . 68 GLN CA C 56.1 . 1 455 . 68 GLN CB C 29.1 . 1 456 . 68 GLN CG C 33.6 . 1 457 . 68 GLN N N 120.9 . 1 458 . 69 GLN H H 8.49 . 1 459 . 69 GLN HA H 4.69 . 1 460 . 69 GLN HB2 H 1.95 . 1 461 . 69 GLN HB3 H 1.95 . 1 462 . 69 GLN HG2 H 2.20 . 2 463 . 69 GLN HG3 H 2.40 . 2 464 . 69 GLN CA C 55.4 . 1 465 . 69 GLN CB C 30.9 . 1 466 . 69 GLN CG C 33.6 . 1 467 . 69 GLN N N 121.1 . 1 468 . 70 VAL H H 9.35 . 1 469 . 70 VAL HA H 4.55 . 1 470 . 70 VAL HB H 2.08 . 1 471 . 70 VAL HG1 H 0.81 . 2 472 . 70 VAL HG2 H 0.97 . 2 473 . 70 VAL CA C 60.7 . 1 474 . 70 VAL CB C 33.7 . 1 475 . 70 VAL CG1 C 19.9 . 2 476 . 70 VAL CG2 C 21.1 . 2 477 . 70 VAL N N 121.7 . 1 478 . 71 ASP H H 8.58 . 1 479 . 71 ASP HA H 5.25 . 1 480 . 71 ASP HB2 H 2.70 . 2 481 . 71 ASP HB3 H 3.27 . 2 482 . 71 ASP CA C 51.8 . 1 483 . 71 ASP CB C 41.9 . 1 484 . 71 ASP N N 124.1 . 1 485 . 72 PHE H H 8.86 . 1 486 . 72 PHE HA H 3.39 . 1 487 . 72 PHE HB2 H 2.49 . 2 488 . 72 PHE HB3 H 2.69 . 2 489 . 72 PHE CA C 62.2 . 1 490 . 72 PHE N N 119.3 . 1 491 . 73 GLN H H 8.21 . 1 492 . 73 GLN HA H 3.52 . 1 493 . 73 GLN HB2 H 2.06 . 1 494 . 73 GLN HB3 H 2.06 . 1 495 . 73 GLN HG2 H 2.15 . 2 496 . 73 GLN HG3 H 2.20 . 2 497 . 73 GLN CA C 59.8 . 1 498 . 73 GLN CB C 27.9 . 1 499 . 73 GLN CG C 34.2 . 1 500 . 73 GLN N N 116.6 . 1 501 . 74 GLU H H 8.11 . 1 502 . 74 GLU HA H 3.90 . 1 503 . 74 GLU HB2 H 2.24 . 1 504 . 74 GLU HB3 H 2.24 . 1 505 . 74 GLU HG2 H 2.42 . 1 506 . 74 GLU HG3 H 2.42 . 1 507 . 74 GLU CA C 59.2 . 1 508 . 74 GLU CB C 29.6 . 1 509 . 74 GLU N N 119.7 . 1 510 . 75 TYR H H 8.35 . 1 511 . 75 TYR HA H 4.22 . 1 512 . 75 TYR HB2 H 2.94 . 2 513 . 75 TYR HB3 H 3.12 . 2 514 . 75 TYR CA C 60.0 . 1 515 . 75 TYR CB C 36.8 . 1 516 . 75 TYR N N 123.2 . 1 517 . 76 ALA H H 8.08 . 1 518 . 76 ALA HA H 3.23 . 1 519 . 76 ALA HB H 0.89 . 1 520 . 76 ALA CA C 54.9 . 1 521 . 76 ALA CB C 17.1 . 1 522 . 76 ALA N N 112.8 . 1 523 . 77 VAL H H 7.86 . 1 524 . 77 VAL HA H 3.30 . 1 525 . 77 VAL HB H 2.08 . 1 526 . 77 VAL HG1 H 0.77 . 2 527 . 77 VAL HG2 H 0.94 . 2 528 . 77 VAL CA C 66.7 . 1 529 . 77 VAL CB C 31.3 . 1 530 . 77 VAL CG1 C 20.4 . 2 531 . 77 VAL CG2 C 23.4 . 2 532 . 77 VAL N N 117.9 . 1 533 . 78 PHE H H 8.14 . 1 534 . 78 PHE HA H 3.93 . 1 535 . 78 PHE HB2 H 2.60 . 2 536 . 78 PHE HB3 H 2.81 . 2 537 . 78 PHE CA C 55.4 . 1 538 . 78 PHE CB C 39.3 . 1 539 . 78 PHE N N 120.7 . 1 540 . 79 LEU H H 8.04 . 1 541 . 79 LEU HA H 3.82 . 1 542 . 79 LEU HB2 H 2.60 . 1 543 . 79 LEU HB3 H 2.60 . 1 544 . 79 LEU CA C 57.4 . 1 545 . 79 LEU CB C 40.6 . 1 546 . 79 LEU N N 115.2 . 1 547 . 80 ALA H H 8.42 . 1 548 . 80 ALA HA H 3.96 . 1 549 . 80 ALA HB H 1.30 . 1 550 . 80 ALA CA C 51.8 . 1 551 . 80 ALA CB C 17.6 . 1 552 . 80 ALA N N 124.1 . 1 553 . 81 LEU H H 8.37 . 1 554 . 81 LEU HA H 3.90 . 1 555 . 81 LEU HB2 H 1.80 . 4 556 . 81 LEU HB3 H 1.33 . 4 557 . 81 LEU HG H 1.68 . 4 558 . 81 LEU CA C 57.6 . 1 559 . 81 LEU CB C 41.3 . 1 560 . 81 LEU N N 119.2 . 1 561 . 82 ILE H H 8.00 . 1 562 . 82 ILE HA H 3.45 . 1 563 . 82 ILE HB H 1.76 . 1 564 . 82 ILE HG2 H 0.72 . 4 565 . 82 ILE HD1 H 0.72 . 4 566 . 82 ILE CA C 64.8 . 1 567 . 82 ILE CB C 37.3 . 1 568 . 82 ILE CG2 C 16.5 . 4 569 . 82 ILE CD1 C 16.5 . 4 570 . 82 ILE N N 118.7 . 1 571 . 83 THR H H 7.88 . 1 572 . 83 THR HG2 H 0.85 . 1 573 . 83 THR CA C 68.0 . 1 574 . 83 THR CB C 69.1 . 1 575 . 83 THR CG2 C 21.4 . 1 576 . 83 THR N N 117.2 . 1 577 . 84 VAL H H 7.56 . 1 578 . 84 VAL HA H 3.31 . 1 579 . 84 VAL HB H 1.85 . 1 580 . 84 VAL CA C 64.9 . 1 581 . 84 VAL CB C 31.6 . 1 582 . 84 VAL CG1 C 20.3 . 1 583 . 84 VAL CG2 C 20.3 . 1 584 . 84 VAL N N 118.0 . 1 585 . 85 MET H H 7.53 . 1 586 . 85 MET HA H 4.09 . 1 587 . 85 MET HB2 H 2.01 . 1 588 . 85 MET HB3 H 2.01 . 1 589 . 85 MET HG2 H 2.46 . 2 590 . 85 MET HG3 H 2.64 . 2 591 . 85 MET CA C 57.7 . 1 592 . 85 MET CB C 33.4 . 1 593 . 85 MET CG C 32.0 . 1 594 . 85 MET N N 117.5 . 1 595 . 86 CYS H H 7.58 . 1 596 . 86 CYS HA H 4.37 . 1 597 . 86 CYS HB2 H 2.34 . 2 598 . 86 CYS HB3 H 2.45 . 2 599 . 86 CYS CA C 59.2 . 1 600 . 86 CYS CB C 28.1 . 1 601 . 86 CYS N N 115.3 . 1 602 . 87 ASN H H 7.98 . 1 603 . 87 ASN CA C 55.2 . 1 604 . 87 ASN CB C 39.9 . 1 605 . 87 ASN N N 120.0 . 1 606 . 88 ASP H H 8.56 . 1 607 . 88 ASP HA H 4.24 . 1 608 . 88 ASP HB2 H 2.47 . 1 609 . 88 ASP HB3 H 2.47 . 1 610 . 88 ASP CA C 55.9 . 1 611 . 88 ASP CB C 39.8 . 1 612 . 88 ASP N N 120.8 . 1 613 . 89 PHE H H 8.07 . 1 614 . 89 PHE HA H 4.54 . 1 615 . 89 PHE CA C 59.2 . 1 616 . 89 PHE N N 119.1 . 1 617 . 90 PHE H H 7.61 . 1 618 . 90 PHE N N 115.6 . 1 619 . 91 GLN H H 7.68 . 1 620 . 91 GLN HA H 4.12 . 1 621 . 91 GLN HB2 H 1.94 . 2 622 . 91 GLN HB3 H 2.07 . 2 623 . 91 GLN HG2 H 2.29 . 1 624 . 91 GLN HG3 H 2.29 . 1 625 . 91 GLN CA C 56.8 . 1 626 . 91 GLN CG C 33.4 . 1 627 . 91 GLN N N 119.2 . 1 628 . 92 GLY H H 8.23 . 1 629 . 92 GLY HA2 H 3.90 . 1 630 . 92 GLY HA3 H 3.90 . 1 631 . 92 GLY CA C 44.9 . 1 632 . 92 GLY N N 109.9 . 1 633 . 93 CYS H H 7.99 . 1 634 . 93 CYS HA H 4.46 . 1 635 . 93 CYS HB2 H 2.52 . 2 636 . 93 CYS HB3 H 2.62 . 2 637 . 93 CYS CA C 56.6 . 1 638 . 93 CYS CB C 26.9 . 1 639 . 93 CYS N N 120.6 . 1 640 . 95 ASP H H 8.38 . 1 641 . 95 ASP HA H 4.52 . 1 642 . 95 ASP HB2 H 2.62 . 1 643 . 95 ASP HB3 H 2.62 . 1 644 . 95 ASP CA C 53.9 . 1 645 . 95 ASP CB C 40.5 . 1 646 . 95 ASP N N 119.0 . 1 647 . 96 ARG H H 7.85 . 1 648 . 96 ARG HA H 4.55 . 1 649 . 96 ARG HB2 H 1.86 . 4 650 . 96 ARG HG2 H 1.69 . 4 651 . 96 ARG CA C 53.7 . 1 652 . 96 ARG CB C 30.2 . 1 653 . 96 ARG N N 121.9 . 1 stop_ save_ save_shift_set_minor _Saveframe_category assigned_chemical_shifts _Details 'S100A2 minor isoform' loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'S100A2 subunit A' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 CYS H H 8.52 . 1 2 . 2 CYS HA H 4.55 . 1 3 . 2 CYS HB2 H 2.86 . 2 4 . 2 CYS HB3 H 2.94 . 2 5 . 2 CYS CA C 58.5 . 1 6 . 2 CYS CB C 28.5 . 1 7 . 2 CYS N N 121.3 . 1 8 . 3 SER H H 8.94 . 1 9 . 3 SER HA H 4.65 . 1 10 . 3 SER HB2 H 3.82 . 2 11 . 3 SER HB3 H 4.35 . 2 12 . 3 SER CA C 57.4 . 2 13 . 3 SER CB C 65.1 . 1 14 . 3 SER N N 119.3 . 1 15 . 4 SER H H 8.75 . 1 16 . 4 SER CA C 60.2 . 1 17 . 4 SER N N 117.3 . 1 18 . 7 GLN H H 8.06 . 1 19 . 7 GLN HA H 4.07 . 1 20 . 7 GLN HB2 H 2.15 . 1 21 . 7 GLN HB3 H 2.15 . 1 22 . 7 GLN HG2 H 2.48 . 2 23 . 7 GLN HG3 H 2.38 . 2 24 . 7 GLN CA C 58.7 . 1 25 . 7 GLN CB C 28.2 . 1 26 . 7 GLN CG C 33.9 . 1 27 . 7 GLN N N 118.0 . 1 28 . 8 ALA H H 8.21 . 1 29 . 8 ALA HA H 4.10 . 1 30 . 8 ALA HB H 1.55 . 1 31 . 8 ALA CA C 54.9 . 1 32 . 8 ALA CB C 17.1 . 1 33 . 8 ALA N N 123.0 . 1 34 . 9 LEU H H 8.38 . 1 35 . 9 LEU CA C 57.7 . 1 36 . 9 LEU N N 117.8 . 1 37 . 10 ALA H H 8.02 . 1 38 . 10 ALA HA H 4.04 . 1 39 . 10 ALA HB H 1.60 . 1 40 . 10 ALA CA C 55.5 . 1 41 . 10 ALA CB C 17.3 . 1 42 . 10 ALA N N 121.0 . 1 43 . 11 VAL H H 7.98 . 1 44 . 11 VAL HA H 3.81 . 1 45 . 11 VAL HB H 2.37 . 1 46 . 11 VAL HG1 H 0.78 . 2 47 . 11 VAL HG2 H 1.16 . 2 48 . 11 VAL CA C 66.5 . 1 49 . 11 VAL CB C 30.9 . 1 50 . 11 VAL CG1 C 20.4 . 2 51 . 11 VAL CG2 C 22.5 . 2 52 . 11 VAL N N 120.4 . 1 53 . 12 LEU H H 8.30 . 1 54 . 12 LEU HA H 3.95 . 1 55 . 12 LEU CA C 60.5 . 1 56 . 12 LEU CB C 44.9 . 1 57 . 12 LEU N N 124.26 . 1 58 . 13 VAL H H 8.15 . 1 59 . 13 VAL HA H 3.63 . 1 60 . 13 VAL HB H 1.98 . 1 61 . 13 VAL HG1 H 0.44 . 2 62 . 13 VAL HG2 H 0.60 . 2 63 . 13 VAL CA C 66.9 . 1 64 . 13 VAL CB C 31.8 . 1 65 . 13 VAL CG1 C 20.6 . 2 66 . 13 VAL CG2 C 22.6 . 2 67 . 13 VAL N N 120.2 . 1 68 . 14 THR H H 8.92 . 1 69 . 14 THR HA H 4.20 . 1 70 . 14 THR HB H 3.90 . 1 71 . 14 THR HG2 H 1.27 . 1 72 . 14 THR CA C 66.5 . 1 73 . 14 THR CB C 68.7 . 1 74 . 14 THR CG2 C 21.4 . 1 75 . 14 THR N N 116.2 . 1 76 . 15 THR H H 8.47 . 1 77 . 15 THR HA H 4.28 . 1 78 . 15 THR HB H 3.90 . 1 79 . 15 THR HG2 H 1.39 . 1 80 . 15 THR CA C 67.9 . 1 81 . 15 THR CG2 C 21.3 . 1 82 . 15 THR N N 112.2 . 1 83 . 16 PHE H H 7.28 . 1 84 . 16 PHE HA H 3.63 . 1 85 . 16 PHE HB2 H 3.28 . 1 86 . 16 PHE HB3 H 3.28 . 1 87 . 16 PHE CA C 62.0 . 1 88 . 16 PHE CB C 39.1 . 1 89 . 16 PHE N N 122.1 . 1 90 . 17 HIS H H 8.24 . 1 91 . 17 HIS CA C 57.7 . 1 92 . 17 HIS CB C 29.4 . 1 93 . 17 HIS N N 115.8 . 1 94 . 18 LYS H H 7.96 . 1 95 . 18 LYS HA H 3.80 . 1 96 . 18 LYS HB2 H 1.91 . 1 97 . 18 LYS HB3 H 1.91 . 1 98 . 18 LYS HG2 H 1.50 . 4 99 . 18 LYS HG3 H 1.50 . 4 100 . 18 LYS HD2 H 1.50 . 4 101 . 18 LYS HD3 H 1.50 . 4 102 . 18 LYS HE2 H 2.76 . 1 103 . 18 LYS HE3 H 2.76 . 1 104 . 18 LYS CA C 59.1 . 1 105 . 18 LYS CB C 32.1 . 1 106 . 18 LYS CG C 24.2 . 1 107 . 18 LYS CD C 29.2 . 1 108 . 18 LYS CE C 41.7 . 1 109 . 18 LYS N N 119.7 . 1 110 . 19 TYR H H 7.05 . 1 111 . 19 TYR HA H 4.17 . 1 112 . 19 TYR HB2 H 2.42 . 1 113 . 19 TYR HB3 H 2.91 . 1 114 . 19 TYR CA C 59.4 . 1 115 . 19 TYR CB C 40.1 . 1 116 . 19 TYR N N 114.1 . 1 117 . 21 CYS H H 9.15 . 1 118 . 21 CYS HA H 4.11 . 1 119 . 21 CYS CA C 57.8 . 1 120 . 21 CYS N N 123.7 . 1 121 . 22 GLN H H 7.59 . 1 122 . 22 GLN CA C 59.3 . 1 123 . 22 GLN CB C 28.2 . 1 124 . 22 GLN N N 115.6 . 1 125 . 24 GLY H H 8.38 . 1 126 . 24 GLY HA2 H 3.87 . 2 127 . 24 GLY HA3 H 3.68 . 2 128 . 24 GLY CA C 46.3 . 1 129 . 24 GLY N N 112.0 . 1 130 . 25 ASP H H 8.29 . 1 131 . 25 ASP CA C 53.7 . 1 132 . 25 ASP CB C 41.0 . 1 133 . 25 ASP N N 123.1 . 1 134 . 28 LYS H H 7.75 . 1 135 . 28 LYS CA C 55.5 . 1 136 . 28 LYS CB C 29.2 . 1 137 . 28 LYS N N 119.3 . 1 138 . 29 LEU H H 7.67 . 1 139 . 29 LEU N N 115.3 . 1 140 . 30 SER H H 9.13 . 1 141 . 30 SER HA H 4.90 . 1 142 . 30 SER HB2 H 4.41 . 2 143 . 30 SER HB3 H 3.95 . 2 144 . 30 SER CA C 57.2 . 1 145 . 30 SER CB C 64.7 . 1 146 . 30 SER N N 119.8 . 1 147 . 31 LYS H H 8.94 . 1 148 . 31 LYS HA H 3.79 . 1 149 . 31 LYS CA C 61.3 . 1 150 . 31 LYS N N 122.3 . 1 151 . 32 GLY H H 8.90 . 1 152 . 32 GLY HA2 H 3.80 . 2 153 . 32 GLY HA3 H 3.98 . 2 154 . 32 GLY CA C 46.8 . 1 155 . 32 GLY N N 105.9 . 1 156 . 33 GLU H H 7.92 . 1 157 . 33 GLU HA H 4.18 . 1 158 . 33 GLU HB2 H 2.32 . 1 159 . 33 GLU HB3 H 2.32 . 1 160 . 33 GLU HG2 H 2.38 . 1 161 . 33 GLU HG3 H 2.38 . 1 162 . 33 GLU CA C 58.4 . 1 163 . 33 GLU CB C 29.3 . 1 164 . 33 GLU CG C 36.6 . 1 165 . 33 GLU N N 124.0 . 1 166 . 34 MET H H 8.51 . 1 167 . 34 MET HA H 4.00 . 1 168 . 34 MET HG2 H 2.27 . 1 169 . 34 MET HG3 H 2.13 . 1 170 . 34 MET CA C 57.7 . 1 171 . 34 MET CB C 31.5 . 1 172 . 34 MET CG C 32.4 . 1 173 . 34 MET N N 120.2 . 1 174 . 35 LYS H H 8.06 . 1 175 . 35 LYS HA H 3.55 . 1 176 . 35 LYS HB2 H 1.93 . 1 177 . 35 LYS HB3 H 1.93 . 1 178 . 35 LYS HG2 H 1.58 . 4 179 . 35 LYS HG3 H 1.58 . 4 180 . 35 LYS HD2 H 1.58 . 4 181 . 35 LYS HD3 H 1.58 . 4 182 . 35 LYS CA C 60.7 . 1 183 . 35 LYS N N 118.8 . 1 184 . 36 GLU H H 7.26 . 1 185 . 36 GLU HA H 4.03 . 1 186 . 36 GLU HB2 H 1.95 . 2 187 . 36 GLU HB3 H 2.12 . 2 188 . 36 GLU HG2 H 2.37 . 1 189 . 36 GLU HG3 H 2.37 . 1 190 . 36 GLU CA C 59.2 . 1 191 . 36 GLU CB C 28.9 . 1 192 . 36 GLU CG C 35.2 . 1 193 . 36 GLU N N 119.0 . 1 194 . 37 LEU H H 8.00 . 1 195 . 37 LEU HA H 4.61 . 1 196 . 37 LEU HB2 H 1.69 . 4 197 . 37 LEU HB3 H 1.69 . 4 198 . 37 LEU HG H 1.69 . 4 199 . 37 LEU HD1 H 1.69 . 4 200 . 37 LEU HD2 H 1.69 . 4 201 . 37 LEU CA C 59.1 . 1 202 . 37 LEU CB C 41.7 . 1 203 . 37 LEU N N 122.0 . 1 204 . 38 LEU H H 8.16 . 1 205 . 38 LEU HA H 3.55 . 1 206 . 38 LEU HB2 H 1.88 . 1 207 . 38 LEU HB3 H 1.88 . 1 208 . 38 LEU CA C 58.17 . 1 209 . 38 LEU CB C 41.55 . 1 210 . 38 LEU N N 118.7 . 1 211 . 39 HIS H H 7.66 . 1 212 . 39 HIS HA H 4.07 . 1 213 . 39 HIS HB2 H 3.09 . 1 214 . 39 HIS HB3 H 3.09 . 1 215 . 39 HIS CA C 59.3 . 1 216 . 39 HIS CB C 29.3 . 1 217 . 39 HIS N N 113.9 . 1 218 . 40 LYS H H 8.34 . 1 219 . 40 LYS HA H 4.10 . 1 220 . 40 LYS HB2 H 2.04 . 1 221 . 40 LYS HB3 H 2.04 . 1 222 . 40 LYS HG2 H 1.74 . 4 223 . 40 LYS HG3 H 1.74 . 4 224 . 40 LYS HD2 H 1.47 . 4 225 . 40 LYS HD3 H 1.47 . 4 226 . 40 LYS HE2 H 3.00 . 1 227 . 40 LYS HE3 H 3.00 . 1 228 . 40 LYS CA C 58.1 . 1 229 . 40 LYS CB C 33.4 . 1 230 . 40 LYS CG C 25.4 . 1 231 . 40 LYS CD C 28.4 . 1 232 . 40 LYS CE C 41.9 . 1 233 . 40 LYS N N 116.0 . 1 234 . 41 GLU H H 8.77 . 1 235 . 41 GLU HA H 4.66 . 1 236 . 41 GLU HB2 H 1.94 . 1 237 . 41 GLU HB3 H 1.94 . 1 238 . 41 GLU CA C 55.4 . 1 239 . 41 GLU CB C 30.3 . 1 240 . 41 GLU CG C 34.9 . 1 241 . 42 LEU H H 7.26 . 1 242 . 42 LEU HA H 5.08 . 1 243 . 42 LEU HB2 H 2.12 . 1 244 . 42 LEU CA C 52.6 . 1 245 . 42 LEU CB C 41.3 . 1 246 . 42 LEU N N 118.2 . 1 247 . 45 PHE H H 8.08 . 1 248 . 45 PHE HA H 4.44 . 1 249 . 45 PHE HB2 H 2.97 . 2 250 . 45 PHE HB3 H 3.07 . 2 251 . 45 PHE CA C 57.6 . 1 252 . 45 PHE CB C 38.3 . 1 253 . 45 PHE N N 122.2 . 1 254 . 46 VAL H H 7.78 . 1 255 . 46 VAL HA H 3.99 . 1 256 . 46 VAL HB H 2.07 . 1 257 . 46 VAL HG1 H 0.76 . 2 258 . 46 VAL HG2 H 0.64 . 2 259 . 46 VAL CA C 62.5 . 1 260 . 46 VAL CB C 32.1 . 1 261 . 46 VAL CG1 C 20.7 . 1 262 . 46 VAL CG2 C 20.7 . 1 263 . 46 VAL N N 114.2 . 1 264 . 47 GLY H H 7.85 . 1 265 . 47 GLY HA2 H 3.93 . 2 266 . 47 GLY HA3 H 4.07 . 2 267 . 47 GLY CA C 46.2 . 1 268 . 47 GLY N N 108.4 . 1 269 . 48 GLU H H 8.02 . 1 270 . 48 GLU HA H 4.31 . 1 271 . 48 GLU HB2 H 2.05 . 1 272 . 48 GLU HB3 H 2.05 . 1 273 . 48 GLU HG2 H 2.25 . 1 274 . 48 GLU HG3 H 2.25 . 1 275 . 48 GLU CA C 57.5 . 1 276 . 48 GLU CB C 29.9 . 1 277 . 48 GLU CG C 36.0 . 1 278 . 48 GLU N N 118.0 . 1 279 . 49 LYS H H 7.92 . 1 280 . 49 LYS HA H 4.44 . 1 281 . 49 LYS HB2 H 1.67 . 2 282 . 49 LYS HB3 H 1.83 . 2 283 . 49 LYS HG2 H 1.56 . 4 284 . 49 LYS HG3 H 1.56 . 4 285 . 49 LYS HD2 H 1.28 . 4 286 . 49 LYS HD3 H 1.28 . 4 287 . 49 LYS HE2 H 2.86 . 1 288 . 49 LYS HE3 H 2.86 . 1 289 . 49 LYS CA C 55.9 . 1 290 . 49 LYS CB C 32.7 . 1 291 . 49 LYS CG C 24.1 . 4 292 . 49 LYS CD C 28.3 . 4 293 . 49 LYS CE C 42.2 . 1 294 . 49 LYS N N 118.3 . 1 295 . 50 VAL H H 7.50 . 1 296 . 50 VAL HA H 4.08 . 1 297 . 50 VAL HB H 2.09 . 1 298 . 50 VAL HG1 H 0.90 . 1 299 . 50 VAL HG2 H 0.90 . 1 300 . 50 VAL CA C 62.3 . 1 301 . 50 VAL CB C 32.6 . 1 302 . 50 VAL CG1 C 20.5 . 1 303 . 50 VAL CG2 C 20.5 . 1 304 . 50 VAL N N 117.8 . 1 305 . 51 ASP H H 8.16 . 1 306 . 51 ASP HA H 4.69 . 1 307 . 51 ASP HB2 H 2.60 . 2 308 . 51 ASP HB3 H 2.81 . 2 309 . 51 ASP CA C 53.5 . 1 310 . 51 ASP CB C 40.9 . 1 311 . 51 ASP N N 121.2 . 1 312 . 52 GLU H H 8.02 . 1 313 . 52 GLU HA H 4.07 . 1 314 . 52 GLU HB2 H 2.15 . 1 315 . 52 GLU HB3 H 2.15 . 1 316 . 52 GLU HG2 H 2.26 . 2 317 . 52 GLU HG3 H 2.37 . 2 318 . 52 GLU CA C 57.9 . 1 319 . 52 GLU CB C 29.7 . 1 320 . 52 GLU CG C 36.4 . 1 321 . 52 GLU N N 123.1 . 1 322 . 53 GLU H H 8.71 . 1 323 . 53 GLU HA H 3.90 . 1 324 . 53 GLU HB2 H 2.00 . 1 325 . 53 GLU HB3 H 2.00 . 1 326 . 53 GLU HG2 H 2.25 . 1 327 . 53 GLU HG3 H 2.25 . 1 328 . 53 GLU CA C 59.4 . 1 329 . 53 GLU CB C 29.3 . 1 330 . 53 GLU CG C 35.6 . 1 331 . 53 GLU N N 123.1 . 1 332 . 54 GLY H H 8.84 . 1 333 . 54 GLY HA2 H 3.78 . 2 334 . 54 GLY HA3 H 3.93 . 2 335 . 54 GLY CA C 47.2 . 1 336 . 54 GLY N N 108.3 . 1 337 . 55 LEU H H 7.90 . 1 338 . 55 LEU CA C 57.3 . 1 339 . 55 LEU CB C 41.5 . 1 340 . 55 LEU N N 124.0 . 1 341 . 56 LYS H H 8.22 . 1 342 . 56 LYS HA H 3.85 . 1 343 . 56 LYS HB2 H 1.80 . 4 344 . 56 LYS HB3 H 1.80 . 4 345 . 56 LYS HG2 H 1.80 . 4 346 . 56 LYS HG3 H 1.80 . 4 347 . 56 LYS HD2 H 1.80 . 4 348 . 56 LYS HD3 H 1.80 . 4 349 . 56 LYS CA C 59.7 . 1 350 . 56 LYS CB C 31.8 . 1 351 . 56 LYS CG C 24.5 . 4 352 . 56 LYS CD C 24.5 . 4 353 . 56 LYS N N 120.0 . 1 354 . 57 LYS H H 7.96 . 1 355 . 57 LYS HA H 4.01 . 1 356 . 57 LYS HB2 H 1.84 . 1 357 . 57 LYS HB3 H 1.84 . 1 358 . 57 LYS HG2 H 1.59 . 4 359 . 57 LYS HG3 H 1.59 . 4 360 . 57 LYS HD2 H 1.33 . 4 361 . 57 LYS HD3 H 1.48 . 4 362 . 57 LYS HE2 H 2.88 . 1 363 . 57 LYS HE3 H 2.88 . 1 364 . 57 LYS CA C 59.2 . 1 365 . 57 LYS CB C 31.9 . 1 366 . 57 LYS CG C 24.3 . 1 367 . 57 LYS CD C 28.7 . 1 368 . 57 LYS CE C 41.6 . 1 369 . 57 LYS N N 119.8 . 1 370 . 58 LEU H H 7.64 . 1 371 . 58 LEU HA H 4.13 . 1 372 . 58 LEU HB2 H 1.70 . 4 373 . 58 LEU HB3 H 1.70 . 4 374 . 58 LEU HG H 1.70 . 4 375 . 58 LEU CA C 58.1 . 1 376 . 58 LEU CG C 24.3 . 1 377 . 58 LEU N N 121.5 . 1 378 . 59 MET H H 8.85 . 1 379 . 59 MET HA H 4.28 . 1 380 . 59 MET HB2 H 2.14 . 1 381 . 59 MET HB3 H 2.14 . 1 382 . 59 MET HG2 H 2.50 . 2 383 . 59 MET HG3 H 2.70 . 2 384 . 59 MET CA C 57.3 . 1 385 . 59 MET CB C 30.8 . 1 386 . 59 MET CG C 32.5 . 1 387 . 59 MET N N 117.7 . 1 388 . 60 GLY H H 8.28 . 1 389 . 60 GLY HA2 H 3.96 . 1 390 . 60 GLY HA3 H 3.96 . 1 391 . 60 GLY CA C 46.5 . 1 392 . 60 GLY N N 107.8 . 1 393 . 61 SER H H 7.78 . 1 394 . 61 SER HA H 4.73 . 1 395 . 61 SER HB2 H 4.12 . 1 396 . 61 SER HB3 H 4.12 . 1 397 . 61 SER CA C 61.1 . 1 398 . 61 SER CB C 62.7 . 1 399 . 61 SER N N 117.3 . 1 400 . 62 LEU H H 7.53 . 1 401 . 62 LEU HA H 4.14 . 1 402 . 62 LEU HB2 H 1.90 . 4 403 . 62 LEU HB3 H 1.77 . 4 404 . 62 LEU HG H 1.77 . 4 405 . 62 LEU HD1 H 1.77 . 4 406 . 62 LEU HD2 H 1.77 . 4 407 . 62 LEU CA C 56.3 . 1 408 . 62 LEU CB C 40.4 . 1 409 . 62 LEU N N 121.5 . 1 410 . 63 ASP H H 7.39 . 1 411 . 63 ASP HA H 4.47 . 1 412 . 63 ASP HB2 H 2.60 . 2 413 . 63 ASP HB3 H 2.76 . 2 414 . 63 ASP CA C 55.1 . 1 415 . 63 ASP CB C 41.1 . 1 416 . 63 ASP N N 116.2 . 1 417 . 64 GLU H H 7.47 . 1 418 . 64 GLU HA H 4.18 . 1 419 . 64 GLU HB2 H 1.98 . 1 420 . 64 GLU HB3 H 1.98 . 1 421 . 64 GLU HG2 H 2.18 . 1 422 . 64 GLU HG3 H 2.18 . 1 423 . 64 GLU CA C 56.2 . 1 424 . 64 GLU CB C 30.2 . 1 425 . 64 GLU CG C 35.7 . 1 426 . 64 GLU N N 119.5 . 1 427 . 65 ASN H H 8.35 . 1 428 . 65 ASN HA H 4.70 . 1 429 . 65 ASN HB2 H 2.89 . 2 430 . 65 ASN HB3 H 2.73 . 2 431 . 65 ASN CA C 53.3 . 1 432 . 65 ASN CB C 37.8 . 1 433 . 65 ASN N N 118.7 . 1 434 . 66 SER H H 8.02 . 1 435 . 66 SER HA H 4.73 . 1 436 . 66 SER HB2 H 4.12 . 1 437 . 66 SER HB3 H 4.12 . 1 438 . 66 SER CA C 61.1 . 1 439 . 66 SER CB C 63.3 . 1 440 . 66 SER N N 115.2 . 1 441 . 67 ASP H H 8.57 . 1 442 . 67 ASP HA H 4.65 . 1 443 . 67 ASP HB2 H 2.70 . 1 444 . 67 ASP HB3 H 2.70 . 1 445 . 67 ASP CA C 54.1 . 1 446 . 67 ASP CB C 40.2 . 1 447 . 67 ASP N N 118.3 . 1 448 . 68 GLN H H 7.90 . 1 449 . 68 GLN HA H 4.23 . 1 450 . 68 GLN HB2 H 2.11 . 1 451 . 68 GLN HB3 H 2.11 . 1 452 . 68 GLN HG2 H 2.49 . 1 453 . 68 GLN HG3 H 2.49 . 1 454 . 68 GLN CA C 56.1 . 1 455 . 68 GLN CB C 29.1 . 1 456 . 68 GLN CG C 33.6 . 1 457 . 68 GLN N N 120.9 . 1 458 . 69 GLN H H 8.49 . 1 459 . 69 GLN HA H 4.69 . 1 460 . 69 GLN HB2 H 1.95 . 1 461 . 69 GLN HB3 H 1.95 . 1 462 . 69 GLN HG2 H 2.20 . 2 463 . 69 GLN HG3 H 2.40 . 2 464 . 69 GLN CA C 55.4 . 1 465 . 69 GLN CB C 30.9 . 1 466 . 69 GLN CG C 33.6 . 1 467 . 69 GLN N N 121.1 . 1 468 . 70 VAL H H 9.40 . 1 469 . 70 VAL HA H 4.55 . 1 470 . 70 VAL HB H 2.08 . 1 471 . 70 VAL HG1 H 0.81 . 2 472 . 70 VAL HG2 H 0.97 . 2 473 . 70 VAL CA C 60.7 . 1 474 . 70 VAL CB C 33.7 . 1 475 . 70 VAL CG1 C 19.9 . 2 476 . 70 VAL CG2 C 21.1 . 2 477 . 70 VAL N N 121.5 . 1 478 . 71 ASP H H 8.56 . 1 479 . 71 ASP HA H 5.25 . 1 480 . 71 ASP HB2 H 2.70 . 2 481 . 71 ASP HB3 H 3.27 . 2 482 . 71 ASP CA C 51.8 . 1 483 . 71 ASP CB C 41.9 . 1 484 . 71 ASP N N 124.0 . 1 485 . 72 PHE H H 9.05 . 1 486 . 72 PHE HA H 3.39 . 1 487 . 72 PHE HB2 H 2.49 . 2 488 . 72 PHE HB3 H 2.69 . 2 489 . 72 PHE CA C 62.2 . 1 490 . 72 PHE N N 119.3 . 1 491 . 73 GLN H H 8.21 . 1 492 . 73 GLN HA H 3.52 . 1 493 . 73 GLN HB2 H 2.06 . 1 494 . 73 GLN HB3 H 2.06 . 1 495 . 73 GLN HG2 H 2.15 . 2 496 . 73 GLN HG3 H 2.20 . 2 497 . 73 GLN CA C 59.8 . 1 498 . 73 GLN CB C 27.9 . 1 499 . 73 GLN CG C 34.2 . 1 500 . 73 GLN N N 116.6 . 1 501 . 74 GLU H H 8.11 . 1 502 . 74 GLU HA H 3.90 . 1 503 . 74 GLU HB2 H 2.24 . 1 504 . 74 GLU HB3 H 2.24 . 1 505 . 74 GLU HG2 H 2.42 . 1 506 . 74 GLU HG3 H 2.42 . 1 507 . 74 GLU CA C 59.2 . 1 508 . 74 GLU CB C 29.6 . 1 509 . 74 GLU N N 119.7 . 1 510 . 75 TYR H H 8.35 . 1 511 . 75 TYR HA H 4.22 . 1 512 . 75 TYR HB2 H 2.94 . 2 513 . 75 TYR HB3 H 3.12 . 2 514 . 75 TYR CA C 60.0 . 1 515 . 75 TYR CB C 36.8 . 1 516 . 75 TYR N N 123.2 . 1 517 . 76 ALA H H 8.08 . 1 518 . 76 ALA HA H 3.23 . 1 519 . 76 ALA HB H 0.89 . 1 520 . 76 ALA CA C 54.9 . 1 521 . 76 ALA CB C 17.1 . 1 522 . 76 ALA N N 112.8 . 1 523 . 77 VAL H H 7.86 . 1 524 . 77 VAL HA H 3.30 . 1 525 . 77 VAL HB H 2.08 . 1 526 . 77 VAL HG1 H 0.77 . 2 527 . 77 VAL HG2 H 0.94 . 2 528 . 77 VAL CA C 66.7 . 1 529 . 77 VAL CB C 31.3 . 1 530 . 77 VAL CG1 C 20.4 . 2 531 . 77 VAL CG2 C 23.4 . 2 532 . 77 VAL N N 117.9 . 1 533 . 78 PHE H H 8.14 . 1 534 . 78 PHE HA H 3.93 . 1 535 . 78 PHE HB2 H 2.60 . 2 536 . 78 PHE HB3 H 2.81 . 2 537 . 78 PHE CA C 55.4 . 1 538 . 78 PHE CB C 39.3 . 1 539 . 78 PHE N N 120.7 . 1 540 . 79 LEU H H 8.04 . 1 541 . 79 LEU HA H 3.82 . 1 542 . 79 LEU HB2 H 2.60 . 1 543 . 79 LEU HB3 H 2.60 . 1 544 . 79 LEU CA C 57.4 . 1 545 . 79 LEU CB C 40.6 . 1 546 . 79 LEU N N 115.2 . 1 547 . 80 ALA H H 8.42 . 1 548 . 80 ALA HA H 3.96 . 1 549 . 80 ALA HB H 1.30 . 1 550 . 80 ALA CA C 51.8 . 1 551 . 80 ALA CB C 17.6 . 1 552 . 80 ALA N N 124.1 . 1 553 . 81 LEU H H 8.37 . 1 554 . 81 LEU HA H 3.90 . 1 555 . 81 LEU HB2 H 1.80 . 4 556 . 81 LEU HB3 H 1.33 . 4 557 . 81 LEU HG H 1.68 . 4 558 . 81 LEU CA C 57.6 . 1 559 . 81 LEU CB C 41.3 . 1 560 . 81 LEU N N 119.2 . 1 561 . 82 ILE H H 8.00 . 1 562 . 82 ILE HA H 3.45 . 1 563 . 82 ILE HB H 1.76 . 1 564 . 82 ILE HG2 H 0.72 . 4 565 . 82 ILE HD1 H 0.72 . 4 566 . 82 ILE CA C 64.8 . 1 567 . 82 ILE CB C 37.3 . 1 568 . 82 ILE CG2 C 16.5 . 4 569 . 82 ILE CD1 C 16.5 . 4 570 . 82 ILE N N 118.7 . 1 571 . 83 THR H H 7.88 . 1 572 . 83 THR HG2 H 0.85 . 1 573 . 83 THR CA C 68.0 . 1 574 . 83 THR CB C 69.1 . 1 575 . 83 THR CG2 C 21.4 . 1 576 . 83 THR N N 117.2 . 1 577 . 84 VAL H H 7.56 . 1 578 . 84 VAL HA H 3.31 . 1 579 . 84 VAL HB H 1.85 . 1 580 . 84 VAL CA C 64.9 . 1 581 . 84 VAL CB C 31.6 . 1 582 . 84 VAL CG1 C 20.3 . 1 583 . 84 VAL CG2 C 20.3 . 1 584 . 84 VAL N N 118.0 . 1 585 . 85 MET H H 7.50 . 1 586 . 85 MET HA H 4.09 . 1 587 . 85 MET HB2 H 2.01 . 1 588 . 85 MET HB3 H 2.01 . 1 589 . 85 MET HG2 H 2.46 . 2 590 . 85 MET HG3 H 2.64 . 2 591 . 85 MET CA C 57.7 . 1 592 . 85 MET CB C 33.4 . 1 593 . 85 MET CG C 32.0 . 1 594 . 85 MET N N 116.7 . 1 595 . 86 CYS H H 7.58 . 1 596 . 86 CYS HA H 4.37 . 1 597 . 86 CYS HB2 H 2.34 . 2 598 . 86 CYS HB3 H 2.45 . 2 599 . 86 CYS CA C 59.2 . 1 600 . 86 CYS CB C 28.1 . 1 601 . 86 CYS N N 115.3 . 1 602 . 87 ASN H H 7.98 . 1 603 . 87 ASN CA C 55.2 . 1 604 . 87 ASN CB C 39.9 . 1 605 . 87 ASN N N 120.0 . 1 606 . 88 ASP H H 8.56 . 1 607 . 88 ASP HA H 4.24 . 1 608 . 88 ASP HB2 H 2.47 . 1 609 . 88 ASP HB3 H 2.47 . 1 610 . 88 ASP CA C 55.9 . 1 611 . 88 ASP CB C 39.8 . 1 612 . 88 ASP N N 120.8 . 1 613 . 89 PHE H H 8.07 . 1 614 . 89 PHE HA H 4.54 . 1 615 . 89 PHE CA C 59.2 . 1 616 . 89 PHE N N 119.1 . 1 617 . 90 PHE H H 7.61 . 1 618 . 90 PHE N N 115.6 . 1 619 . 91 GLN H H 7.68 . 1 620 . 91 GLN HA H 4.12 . 1 621 . 91 GLN HB2 H 1.94 . 2 622 . 91 GLN HB3 H 2.07 . 2 623 . 91 GLN HG2 H 2.29 . 1 624 . 91 GLN HG3 H 2.29 . 1 625 . 91 GLN CA C 56.8 . 1 626 . 91 GLN CG C 33.4 . 1 627 . 91 GLN N N 119.2 . 1 628 . 92 GLY H H 8.23 . 1 629 . 92 GLY HA2 H 3.90 . 1 630 . 92 GLY HA3 H 3.90 . 1 631 . 92 GLY CA C 44.9 . 1 632 . 92 GLY N N 109.9 . 1 633 . 93 CYS H H 7.99 . 1 634 . 93 CYS HA H 4.46 . 1 635 . 93 CYS HB2 H 2.52 . 2 636 . 93 CYS HB3 H 2.62 . 2 637 . 93 CYS CA C 56.6 . 1 638 . 93 CYS CB C 26.9 . 1 639 . 93 CYS N N 120.6 . 1 640 . 95 ASP H H 8.17 . 1 641 . 95 ASP HA H 4.52 . 1 642 . 95 ASP HB2 H 2.62 . 1 643 . 95 ASP HB3 H 2.62 . 1 644 . 95 ASP CA C 54.2 . 1 645 . 95 ASP CB C 40.7 . 1 646 . 95 ASP N N 119.8 . 1 647 . 96 ARG H H 7.94 . 1 648 . 96 ARG HA H 4.55 . 1 649 . 96 ARG HB2 H 1.86 . 4 650 . 96 ARG HG2 H 1.69 . 4 651 . 96 ARG CA C 53.5 . 1 652 . 96 ARG CB C 30.1 . 1 653 . 96 ARG N N 121.6 . 1 stop_ save_